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1 , which confer quaternary flexibility to the multienzyme complex.
2 Glu462 increases the thermostability of the multienzyme complex.
3 mbly of the cellulosomal components into the multienzyme complex.
4 mponents of the 2-oxoglutarate dehydrogenase multienzyme complex.
5 onents of the E. coli pyruvate dehydrogenase multienzyme complex.
6 omponent of the human pyruvate dehydrogenase multienzyme complex.
7 pyruvate by the pyruvate dehydrogenase (PDH) multienzyme complex.
8 ications are believed to be carried out by a multienzyme complex.
9 gluconeogenesis, supporting the formation of multienzyme complexes.
10 e additional flexibility in highly populated multienzyme complexes.
11 rix, are interchangeable among the different multienzyme complexes.
12 integral component of the function of these multienzyme complexes.
13 that react with components of mitochondrial multienzyme complexes.
14 the quaternary structure of highly populated multienzyme complexes.
15 ote cell proliferation often proceed through multienzyme complexes.
16 cal role in stabilizing and regulating these multienzyme complexes.
17 mes, but via one or more membrane-associated multienzyme complexes.
18 ns catalysed by the 2-oxo acid dehydrogenase multienzyme complexes.
19 utarate dehydrogenase, and glycine reductase multienzyme complexes.
20 utarate dehydrogenase, and glycine reductase multienzyme complexes.
21 tute for mtLPD2 and associate with all these multienzyme complexes.
22 (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes.
23 scherichia coli 1-lip pyruvate dehydrogenase multienzyme complex (1-lip PDHc) with the C259N and C259
25 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze
26 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase that catalyze
27 lation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase, which cataly
28 th variants displayed pyruvate dehydrogenase multienzyme complex activity at levels of 11% (Y177A E1)
29 us stearothermophilus pyruvate dehydrogenase multienzyme complex adopts a unique, compact structure.
30 ated the composition and organization of the multienzyme complex alpha-ketoglutarate dehydrogenase (a
31 ering the understanding of its function in a multienzyme complex and in the membrane-bound P64K prote
32 performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial ta
33 dmark structure was the first structure of a multienzyme complex and the first structure revealing an
34 s about the functional significance of these multienzyme complexes and whether they might play a more
35 branched chain alpha-ketoacid dehydrogenase multienzyme complex (approximately 4-5 x 10(3) kDa) is a
36 t of Escherichia coli pyruvate dehydrogenase multienzyme complex are essential for several catalytic
38 he pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes are specifically recognised by the
40 utida and P. aeruginosa encode the inducible multienzyme complex branched-chain keto acid dehydrogena
41 type activity levels for E3 and all affected multienzyme complexes but are phenotypically normal.
43 for its growth and produces an extracellular multienzyme complex called the cellulosome, which is inv
44 he entire assembly and characterization of a multienzyme complex can be completed within 1-2 weeks.
47 nformation regarding recognition within this multienzyme complex class with an alpha(2) E1 assembly.
48 the entire family of homodimeric (alpha2) E1 multienzyme complex components, and should serve as a mo
49 lar eukaryotes, one of these assemblies is a multienzyme complex composed of eight proteins that have
50 integral component of T4 dNTP synthetase, a multienzyme complex containing phage-coded enzymes, whic
51 The Escherichia coli pyruvate dehydrogenase multienzyme complex contains multiple copies of three en
52 s by E3 or E1, respectively, showed that the multienzyme complex does not behave as a simple competit
53 domains of E1p relative to heterotetrameric multienzyme complex E1 components operating on branched
54 gnment of the E. coli pyruvate dehydrogenase multienzyme complex E1 subunit and yeast transketolase c
55 two enzymes are found in dNTP synthetase, a multienzyme complex for deoxyribonucleotide biosynthesis
56 virus (mORV) core particle is an icosahedral multienzyme complex for viral mRNA synthesis and provide
57 ipoyl cofactor, which is employed by several multienzyme complexes for the oxidative decarboxylation
58 from the family of 2-oxo acid dehydrogenase multienzyme complexes form large protein scaffolds, to w
59 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex found in methanogens and certain oth
60 (E2) component of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus is
62 ranscarboxylase is a 1.2 million Dalton (Da) multienzyme complex from Propionibacterium shermanii tha
65 ence that cell wall synthesis is mediated by multienzyme complexes; however, our results suggest that
68 restingly, GSK3beta can be released from the multienzyme complex in response to PKA phosphorylation o
70 quivalent domain in a pyruvate dehydrogenase multienzyme complex in which the domain remains of const
71 hesis seems to be spatially regulated by the multienzyme complexes in a cluster-size-dependent manner
72 bition method may be a powerful way to study multienzyme complexes in their physiological context.
73 anched-chain keto acid dehydrogenase (BCKAD) multienzyme complex involved in branched-chain fatty aci
74 ofactor required for the function of several multienzyme complexes involved in the oxidative decarbox
75 the Escherichia coli pyruvate dehydrogenase multienzyme complex is an outcome of redistribution of a
76 omponent of the 2-oxoglutarate dehydrogenase multienzyme complex is composed of 24 subunits arranged
78 tion are still unknown, but the formation of multienzyme complexes is considered a feasible Golgi pro
79 encoding three alpha-ketoacid dehydrogenase multienzyme complexes (KADHs) that have central metaboli
82 rogenase complex (PDC) is one of the largest multienzyme complexes known and consists of a dodecahedr
84 polypeptide from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus assem
85 omponent of the pyruvate dehydrogenase (PDH) multienzyme complex of Bacillus stearothermophilus has i
89 rase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli is catalysed spe
90 de chain of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli was over-express
91 Glu139 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri
92 His450 of the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escheri
95 es of the human 2-oxoglutarate dehydrogenase multienzyme complex (OGDHc), a rate-limiting enzyme in t
96 shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human eryt
97 ic enzymes (GEs) have been shown to exist in multienzyme complexes on the inner surface of the human
98 2) phosphorylates the pyruvate dehydrogenase multienzyme complex (PDC) and thereby controls the rate
102 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) and its E1 (ThDP-dependent) c
103 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) by its coenzyme thiamin dipho
104 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined at a reso
105 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc) has been determined with phos
106 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), as a representative of the P
107 the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), binds to the enzyme with gre
108 The Escherichia coli pyruvate dehydrogenase multienzyme complex (PDHc), consisting of multiple copie
109 dihydrolipoyl moieties of four mitochondrial multienzyme complexes: pyruvate dehydrogenase, alpha-ket
110 essential cofactor for several mitochondrial multienzyme complexes required for oxidative metabolism.
113 quired for the function of several essential multienzyme complexes, such as pyruvate dehydrogenase (P
114 H are structurally and catalytically similar multienzyme complexes, suggesting a common mode of inhib
116 herichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of s
117 icrobes, cellulases are assembled into large multienzymes complexes, termed "cellulosomes," which all
118 th subunits of the fatty acid beta-oxidation multienzyme complex that are normally present in the mat
119 rom Propionibacterium shermanii is a 1.2 MDa multienzyme complex that couples two carboxylation react
120 oduces the prototypical cellulosome, a large multienzyme complex that efficiently hydrolyzes plant ce
122 al gene copies of the pyruvate dehydrogenase multienzyme complex that have evolved into a pyruvate de
124 troviral protease is a key enzyme in a viral multienzyme complex that initiates an ordered sequence o
125 dy, we demonstrate that this pathway forms a multienzyme complex that is associated with the nuclear
126 etases examined can be isolated as part of a multienzyme complex that is more stable, and consequentl
127 SAHH associates with DAO as part of a larger multienzyme complex that may function in planta as a nic
128 cetyl-CoA decarbonylase/synthase (ACDS) is a multienzyme complex that plays a central role in energy
129 s still carried out, but in the context of a multienzyme complex that remains structurally intact dur
130 onucleoside triphosphate biosynthesis form a multienzyme complex that we call T4 deoxyribonucleoside
131 component of the three functional classes of multienzyme complexes that catalyze the oxidative decarb
132 drogenase is a common component of mammalian multienzyme complexes that decarboxylate alpha-ketoacids
133 tabolism have long been hypothesized to form multienzyme complexes that regulate glucose flux in livi
136 Evidence has been presented for a metabolic multienzyme complex, the purinosome, that participates i
137 e assembly of one of Nature's most elaborate multienzyme complexes, the cellulosome, results from the
139 By linking the MAP3K, MAP2K and MAPK into a multienzyme complex, these MAPK-specific scaffold protei
140 novo purine biosynthetic pathway may form a multienzyme complex to facilitate substrate flux through
141 esized and posttranslationally modified by a multienzyme complex to their biologically active forms.
142 A (PPCA), a serine carboxypeptidase, forms a multienzyme complex with beta-galactosidase and neuramin
143 Lysosomal neuraminidase-1 (NEU1) forms a multienzyme complex with beta-galactosidase and protecti
146 n-regulated chloroplast protein CP12 forms a multienzyme complex with the Calvin-Benson cycle enzymes
147 he nucleus during S-phase, where they form a multienzyme complex with thymidylate synthase (TYMS) and
148 the Escherichia coli pyruvate dehydrogenase multienzyme complex with Y177A and Y177F substitutions w
149 tly involved in the hydratase catalysis, the multienzyme complexes with either an alpha/Asp69 --> Asn
150 oprotein in at least two major mitochondrial multienzyme complexes would be consistent with a role in
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